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Conserved domains on  [gi|7304867|ref|NP_038487|]
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complement factor D isoform 1 preproprotein [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-252 2.49e-83

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 248.73  E-value: 2.49e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867   26 ILGGQEAAAHARPYMASVQVN-GTHVCGGTLLDEQWVLSAAHCMDGvTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867  105 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRT 184
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7304867  185 YHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA----VEGVVTWGSRvCGNGKKPGVYTRVSSYRMWIENI 252
Cdd:cd00190 160 SYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-252 2.49e-83

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 248.73  E-value: 2.49e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867   26 ILGGQEAAAHARPYMASVQVN-GTHVCGGTLLDEQWVLSAAHCMDGvTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867  105 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRT 184
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7304867  185 YHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA----VEGVVTWGSRvCGNGKKPGVYTRVSSYRMWIENI 252
Cdd:cd00190 160 SYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-249 8.67e-79

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 237.19  E-value: 8.67e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867      25 RILGGQEAAAHARPYMASVQVNG-THVCGGTLLDEQWVLSAAHCMDGVtDDDSVQVLLGAHSLSAPEPYKRwYDVQSVVP 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQV-IKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867     104 HPGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTH-AGRRPDVLHQLRVSIMNRTTCNL 182
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7304867     183 RTYHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA---VEGVVTWGSrVCGNGKKPGVYTRVSSYRMWI 249
Cdd:smart00020 159 AYSGGGAITDNMLCAggLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
26-249 4.57e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 217.31  E-value: 4.57e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867     26 ILGGQEAAAHARPYMASVQV-NGTHVCGGTLLDEQWVLSAAHCmdgVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 104
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867    105 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGvVTHAGRRPDVLHQLRVSIMNRTTCnlRT 184
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETC--RS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7304867    185 YHDGVVTINMMCAESNRRDTCRGDSGSPLVCGDA-VEGVVTWGsRVCGNGKKPGVYTRVSSYRMWI 249
Cdd:pfam00089 155 AYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDGeLIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
8-256 3.98e-58

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 185.62  E-value: 3.98e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867    8 VALVILGAAVCAAQPRGRILGGQEAAAHARPYMASVQVNG---THVCGGTLLDEQWVLSAAHCMDGVTDDDsVQVLLGAH 84
Cdd:COG5640  13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD-LRVVIGST 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867   85 SLSAPEPykRWYDVQSVVPHPGSRPDSLEDDLILFKLSQNAslgPHVRPLPLQYEDKEVEPGTLCDVAGWGVV-THAGRR 163
Cdd:COG5640  92 DLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQ 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867  164 PDVLHQLRVSIMNRTTCNlrtYHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDAVE----GVVTWGSRVCGnGKKPG 237
Cdd:COG5640 167 SGTLRKADVPVVSDATCA---AYGGFDGGTMLCAgyPEGGKDACQGDSGGPLVVKDGGGwvlvGVVSWGGGPCA-AGYPG 242
                       250
                ....*....|....*....
gi 7304867  238 VYTRVSSYRMWIENITNGN 256
Cdd:COG5640 243 VYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-252 2.49e-83

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 248.73  E-value: 2.49e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867   26 ILGGQEAAAHARPYMASVQVN-GTHVCGGTLLDEQWVLSAAHCMDGvTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867  105 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRT 184
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7304867  185 YHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA----VEGVVTWGSRvCGNGKKPGVYTRVSSYRMWIENI 252
Cdd:cd00190 160 SYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-249 8.67e-79

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 237.19  E-value: 8.67e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867      25 RILGGQEAAAHARPYMASVQVNG-THVCGGTLLDEQWVLSAAHCMDGVtDDDSVQVLLGAHSLSAPEPYKRwYDVQSVVP 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQV-IKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867     104 HPGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTH-AGRRPDVLHQLRVSIMNRTTCNL 182
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7304867     183 RTYHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA---VEGVVTWGSrVCGNGKKPGVYTRVSSYRMWI 249
Cdd:smart00020 159 AYSGGGAITDNMLCAggLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
26-249 4.57e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 217.31  E-value: 4.57e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867     26 ILGGQEAAAHARPYMASVQV-NGTHVCGGTLLDEQWVLSAAHCmdgVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 104
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867    105 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGvVTHAGRRPDVLHQLRVSIMNRTTCnlRT 184
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETC--RS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7304867    185 YHDGVVTINMMCAESNRRDTCRGDSGSPLVCGDA-VEGVVTWGsRVCGNGKKPGVYTRVSSYRMWI 249
Cdd:pfam00089 155 AYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDGeLIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
8-256 3.98e-58

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 185.62  E-value: 3.98e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867    8 VALVILGAAVCAAQPRGRILGGQEAAAHARPYMASVQVNG---THVCGGTLLDEQWVLSAAHCMDGVTDDDsVQVLLGAH 84
Cdd:COG5640  13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD-LRVVIGST 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867   85 SLSAPEPykRWYDVQSVVPHPGSRPDSLEDDLILFKLSQNAslgPHVRPLPLQYEDKEVEPGTLCDVAGWGVV-THAGRR 163
Cdd:COG5640  92 DLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQ 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867  164 PDVLHQLRVSIMNRTTCNlrtYHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDAVE----GVVTWGSRVCGnGKKPG 237
Cdd:COG5640 167 SGTLRKADVPVVSDATCA---AYGGFDGGTMLCAgyPEGGKDACQGDSGGPLVVKDGGGwvlvGVVSWGGGPCA-AGYPG 242
                       250
                ....*....|....*....
gi 7304867  238 VYTRVSSYRMWIENITNGN 256
Cdd:COG5640 243 VYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
46-232 6.58e-09

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 54.30  E-value: 6.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867   46 NGTHVCGGTLLDEQWVLSAAHCMDGVTDD---DSVQVLLGAHSlsapEPYKRWYDVQSVVpHPGSRPD-SLEDDLILFKL 121
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGgwaTNIVFVPGYNG----GPYGTATATRFRV-PPGWVASgDAGYDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867  122 sqNASLGPHVRPLPLQYEDKEVEPGTlcdvagWGVVTHAGRRPDVLHQlrvsimnRTTCNLRTYHDGVVTINMmcaesnr 201
Cdd:COG3591  84 --DEPLGDTTGWLGLAFNDAPLAGEP------VTIIGYPGDRPKDLSL-------DCSGRVTGVQGNRLSYDC------- 141
                       170       180       190
                ....*....|....*....|....*....|....*
gi 7304867  202 rDTCRGDSGSPLV----CGDAVEGVVTWGSRVCGN 232
Cdd:COG3591 142 -DTTGGSSGSPVLddsdGGGRVVGVHSAGGADRAN 175
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
38-133 1.36e-05

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 43.31  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304867     38 PYMASVQVNGTHVCGGTLLDEQWVLSAAHCMDGVTDDDS-VQVLLGAHS--LSAPEPYKRWYDVQsvvphpgSRPDSLED 114
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQyISVVLGGAKtlKSIEGPYEQIVRVD-------CRHDIPES 74
                          90
                  ....*....|....*....
gi 7304867    115 DLILFKLSQNASLGPHVRP 133
Cdd:pfam09342  75 EISLLHLASPASFSNHVLP 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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